4pa8
From Proteopedia
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==Crystal structure of a de novo retro-aldolase catalyzing asymmetric Michael additions, with a covalently bound product analog== | ==Crystal structure of a de novo retro-aldolase catalyzing asymmetric Michael additions, with a covalently bound product analog== | ||
<StructureSection load='4pa8' size='340' side='right' caption='[[4pa8]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='4pa8' size='340' side='right' caption='[[4pa8]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2K6:(3R)-3-(4-METHOXYPHENYL)-5-OXOHEXANENITRILE'>2K6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2K6:(3R)-3-(4-METHOXYPHENYL)-5-OXOHEXANENITRILE'>2K6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a29|4a29]], [[4a2s|4a2s]], [[4a2r|4a2r]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a29|4a29]], [[4a2s|4a2s]], [[4a2r|4a2r]]</td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pa8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pa8 RCSB], [http://www.ebi.ac.uk/pdbsum/4pa8 PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pa8 OCA], [http://pdbe.org/4pa8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pa8 RCSB], [http://www.ebi.ac.uk/pdbsum/4pa8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pa8 ProSAT]</span></td></tr> |
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4pa8" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Aldolase|Aldolase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 17:27, 9 March 2017
Crystal structure of a de novo retro-aldolase catalyzing asymmetric Michael additions, with a covalently bound product analog
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Categories: Beck, T | Hilvert, D | Pi, X Garrabou | Aldolase | Artificial catalyst | Computer-aided design | De novo protein | Directed evolution | Enzyme design | Enzyme-product analog complex | Hydrolase | Michael addition | Protein engineering | Retro-aldolase | Substrate specificity | Tim-barrel fold
